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dc.contributor.advisorCowan, Don A.
dc.contributor.advisorTuffin, Marla
dc.contributor.advisorvan Zyl, Lonnie
dc.contributor.authorMketsu, Moses Clive Masisange
dc.contributor.otherDept. of Biotechnology
dc.contributor.otherFaculty of Science
dc.date.accessioned2014-01-17T12:49:05Z
dc.date.available2011/06/08 08:31
dc.date.available2011/06/08
dc.date.available2014-01-17T12:49:05Z
dc.date.issued2009
dc.identifier.urihttp://hdl.handle.net/11394/2609
dc.descriptionMagister Scientiae - MScen_US
dc.description.abstractIn this study G. pallidus RAPc8 NHase mutants were screened for reduced substrate inhibition compared to the wild type enzyme. Wild type and mutant enzymes were expressed and purified using hydrophobic interaction chromatography. Amidase coupled enzyme stop assays were conducted using 3-cyanopyridine as a substrate, whereas continuous enzyme kinetics were conducted using acrylonitrile as a substrate.en_US
dc.language.isoenen_US
dc.publisherUniversity of the Western Capeen_US
dc.subjectNitrogen compoundsen_US
dc.subjectNitrilesen_US
dc.subjectNitrogenen_US
dc.titleScreening for subtate tolerant Geobacillus pallidus RAPc8 nitrile hydrataseen_US
dc.typeThesisen_US
dc.rights.holderUniversity of the Western Capeen_US
dc.description.countrySouth Africa


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